3NIP

Crystal structure of Pseudomonas aeruginosa guanidinopropionase complexed with 1,6-diaminohexane

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008783	molecular_function	agmatinase activity
A	0016787	molecular_function	hydrolase activity
A	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
A	0046872	molecular_function	metal ion binding
A	0047972	molecular_function	guanidinopropionase activity
B	0008783	molecular_function	agmatinase activity
B	0016787	molecular_function	hydrolase activity
B	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
B	0046872	molecular_function	metal ion binding
B	0047972	molecular_function	guanidinopropionase activity
C	0008783	molecular_function	agmatinase activity
C	0016787	molecular_function	hydrolase activity
C	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
C	0046872	molecular_function	metal ion binding
C	0047972	molecular_function	guanidinopropionase activity
D	0008783	molecular_function	agmatinase activity
D	0016787	molecular_function	hydrolase activity
D	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
D	0046872	molecular_function	metal ion binding
D	0047972	molecular_function	guanidinopropionase activity
E	0008783	molecular_function	agmatinase activity
E	0016787	molecular_function	hydrolase activity
E	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
E	0046872	molecular_function	metal ion binding
E	0047972	molecular_function	guanidinopropionase activity
F	0008783	molecular_function	agmatinase activity
F	0016787	molecular_function	hydrolase activity
F	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
F	0046872	molecular_function	metal ion binding
F	0047972	molecular_function	guanidinopropionase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 16D B 327

Chain	Residue
B	ARG51
C	VAL298
B	PRO246
B	PRO250
B	PRO255
B	ILE257
C	PHE248
C	GLY292
C	ALA294
C	LEU297

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 16D B 328

Chain	Residue
B	PHE248
B	GLY292
B	ALA294
B	LEU297
B	VAL298
B	HOH369
B	HOH830
E	ARG51
E	PRO246
E	PRO250

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 16D D 327

Chain	Residue
D	ARG51
D	PRO246
D	PRO250
F	PHE248
F	GLY292
F	ALA294
F	LEU297
F	VAL298
F	HOH828

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 16D D 328

Chain	Residue
A	ARG51
A	PRO246
A	PRO250
D	PHE248
D	ALA294
D	LEU297
D	VAL298
D	HOH350
D	HOH356

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 16D E 327

Chain	Residue
C	ARG189
C	GLY190
C	GLU212
C	GLU256
C	ILE257
C	HOH831
E	HIS73
E	GLN266
E	ARG270
E	LEU297
E	THR301

---

Functional Information from PROSITE/UniProt

site_id	PS01053
Number of Residues	22
Details	ARGINASE_1 Arginase family signature. SFDVDvldPafaPGtgtpeigG

Chain	Residue	Details
A	SER238-GLY259

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21600989","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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